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CC MTAP2 > CC (midterms) > Flashcards

CC (midterms) Flashcards

1
Q

Enzymes

A

Biologic proteins that catalyze the biochemical reactions

Intracellular proteins to hasten the chemical reaction

Affects the reaction of organic matter

Enzymes are not consumed nor altered

Only the substrates changes the form (substrate to product)

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2
Q

Increased enzymes in the serum may be because:

A

Cell injury or cell degradation

Increased membrane permeability allowing for proteins to move out of the cell

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3
Q

Function of enzymes:

A

Hydration of carbon dioxide during respiration
Nerve induction
Muscle contraction
Nutrient degradation
Growth and reproduction
Energy storage and use

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4
Q

LIVER ENZYMES

A

Aspartate aminotransferase (AST)
Alanine aminotransferase (ALT)
Gamma-Glutamyl transferase (GGT)
Alkaline phosphatase (ALP)
Acid phosphatase (ACP)

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5
Q

MI Profile

A

Creatine Kinase (CK)
Aspartate Aminotransferase (AST)
Lactate Dehydrogenase (LDH)

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6
Q

Pancreatic Enzymes

A

Amylase (AMS)
Lipase (LPS)

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7
Q

Prostate enzymes

A

Acid phosphatase (ACP)
Glucose-6-phosphate dehydrogenase (G6PDH)

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8
Q

Miscellaneous enzymes

A
  • 5’ Nucleotidase (5’N)
  • Cholinesterase / Pseudocholinesterase
  • Angiotensin-Converting enzyme (ACE)
  • Ceruloplasmin
  • Ornithine carbamoyl Transferase (OCT)
  • Glucose-6-phosphate dehydrogenase (G-6PD)
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9
Q

other name for AST

A

Serum glutamic-oxaloacetic transaminase or Serum glutamate-oxaloacetate transaminase (SGOT)

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10
Q

Transfer of an amino group between aspartate and a-keto acids

A

AST

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11
Q

Involved in the synthesis and degradation of AA (amino acids)

A

AST

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12
Q

Widely distributed, highest activities in cardiac, liver and skeletal muscle

A

AST

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13
Q

2 isoenzymes of AST

A

Cytoplasmic
Mitochondrial

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14
Q

most abundant, the most predominant AST in healthy human serum

A

Cytoplasmic AST

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15
Q

present in the mitochondrial membrane. An increase in this isoenzyme indicates possible necrosis or severe damage of the cell.

A

Mitochondrial AST

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16
Q

After MI, AST levels begin to rise in ___, peak at ___, and return to normal in ____.

A

6–8 hours; 24 hours; 5 days

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17
Q

AST increased in

A

in hepatocellular and skeletal muscle disease

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18
Q

Uses malate dehydrogenase and monitors decrease in absorbance at 340 nm

A

Karmen Method

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19
Q

method that is falsely ↑ in hemolyzed sample

A

Karmen Method

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20
Q

Karmen Method reference range:

A

5-30 U/L

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21
Q

Aspartic acid + a-ketoglutaric acid ⇆ ____________

A

glutamic acid + oxaloacetic acid

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22
Q

oxaloacetate + NADH + H ⇆ _____

A

malate + NAD

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23
Q

are enzymes with similar catalytic activity but differ in the physical, biochemical and immunologic properties.

A

Isoenzymes

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24
Q

a type of cofactor that serves as the second substrate for enzymes.

A

Coenzymes

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25
Q

When a coenzyme is tightly bound to an enzyme, it is called a ____

A

prosthetic group

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26
Q

Oxidized form: NAD measures for

A

Decreased absorbance

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27
Q

Reduced form: NADH

A

high/increased absorbance

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28
Q

other name for Alanine aminotransferase (ALT)

A

serum glutamic-pyruvic transaminase (SGPT)

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29
Q

Transfer of an amino group between alanine and a-ketoglutarate

A

ALT

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30
Q

more liver specific compared to AST

A

ALT

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31
Q

Increased in hepatocellular disorders

A

ALT

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32
Q

Significant in the evaluation of hepatic disorders
Markedly increased in acute inflammatory conditions of the liver
Used to monitor the course of hepatitis treatment and the effects drug therapy
Used for screening for post transfusion hepatitis
Used to screen blood donors, (ALT increased with people with jaundice)
Used as sensitive test for occupational toxic exposure
Monitors course of hepa treatment and possible effects of drug therapy

A

uses of ALT

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33
Q

The AST/ALT Ratio
Differentiates the cause of hepatic disorder

A

De Ritis Ratio

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34
Q

Ratio > 1

A

non viral origin

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35
Q

Ratio < 1

A

viral in origin

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36
Q

pyruvate + NADH + H ⇆ _____

A

Lactate + NAD

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37
Q

pyruvate +glutamate ⇆ _____

A

alanine + a-ketoglutarate

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38
Q

Assay for enzyme activity ALT
Uses Lactate Dehydrogenase and monitors decrease in absorbance at ___

A

340 nm

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39
Q

COLOR DEVELOPER ALT and AST

A

2,4 DNPH

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40
Q

COLOR INTENSIFIER ALT & AST

A

0.4 N NaOH

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41
Q

METHODS for ALT and AST

A

Reitman and Frankel

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42
Q

Catalyze the transfer of the y-glutamyl residue from y-glutamyl peptides to amino acids H2O, etc

A

Gamma-Glutamyl transferase (GGT)

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43
Q

In the biologic system, the common donor for y-glutamyl is _____

A

glutathione

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44
Q

glutathione + amino acid → ___

A

glutamyl-peptide + L-cysteinyglycine

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45
Q

Used for diagnosis hepatobiliary disorders and chronic alcoholism

A

GGT

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46
Q

GGT is located in the ____ of the hepatic cells. Specifically in the epithelial cell linings of _____

A

canaliculi; biliary ductules

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47
Q

Sensitive marker for ethanol intoxication.
Marker for occult alcoholism

A

GGT

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48
Q

Most sensitive marker for acute alcoholic hepatitis

A

GGT

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49
Q

Assay for Enzyme Activity in GGT

A

Szaz Assay

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50
Q

The absorbance of p-Nitroaniline is measured at

A

405-420 nm

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51
Q

y-glutamyl-p-nitroanilide + glycylglycine → ____

A

y-glutamyl-glycylglycine + p-nitroaniline

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52
Q

Involved in the storage of high-energy creatine phosphate in muscle cells

A

Creatine Kinase (CK) or Creatine Phosphokinase (CPK)

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53
Q

CK is widely distributed, highest activities in _____.

A

skeletal muscle, heart and brain.

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54
Q

creatine phosphate + ADP → ___

A

creatine + ATP

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55
Q

Methods of determination for CK

A

Forward Reaction (Tanzer-Gilvarg)
Reverse Reaction (Oliver-Rosalki)

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56
Q

Optimum pH for Tanzer Gilvarg

A

9.0

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57
Q

Optimum pH for Oliver-Rosalki

A

6.8

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58
Q

↓ in absorbance at 340 nm is determined

A

Forward Reaction (Tanzer-Gilvarg)

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59
Q

↑ in absorbance at 340 nm is determined

A

Reverse Reaction (Oliver-Rosalki)

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60
Q

Source of Error for CK

A

Hemolysis
inactivation by light
Physical activity and IM injections

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61
Q

Reference Range of CK (male & female; % of CK-MB)

A

Male: 15-160 U/L; Female: 15-130 U/L
CK-MB: <6% of total CK

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62
Q

Slowest mobility toward the anode
Major isoenzyme in striated muscle and normal serum

A

Ck-3/CK-MM/
Muscle type

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63
Q

2nd fastest to migrate toward the anode
Significant quantities are found in heart tissues

A

CK-2/CK-MB/
Hybrid type

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64
Q

Migrate the fastest toward the anode
Highest concentration in CNS, GI tract and uterus (pregnancy)

A

CK-1/CK-BB/
Brain type

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65
Q

After MI, CK-MB (>6%) levels begin to rise within ___, peak at ____ and return to normal levels within ___

A

4-8 hours; 12-24 hrs; 48-72 hrs

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66
Q

It is the first enzyme to elevate after a myocardial infarction

A

CK

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67
Q

CK is considered a ____ . It is composed of two different monomers. Composed of M and B type

A

dimeric molecule

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68
Q

Reference Values of CKs

A

CK-MM: 94-98%
CK-MB: 2-6%
CK-BB: <1%

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69
Q

Other CK Isoenzymes

A

Macro-CK

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70
Q

CK-BB is complexed with antibodies __

A

IgG or IgA

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71
Q

CK-MM is complexed with ___

A

lipoproteins

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72
Q

macro-CK migrate midway between ___

A

CK-MM and CK-MB

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73
Q

Located in mitochondrial membrane, increase in this indicates cell necrosis or severe damage
Migrates cathodal to CK-MM

A

Mitochondrial CK (CK-Mi)

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74
Q

Where the activity of CK1, CK2 and CK3 are all measured
It is less diagnostic bc it is not tissue specific

A

Total CK

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75
Q

This targets a particular tissue
Improves the test specificity thus improving diagnosis

A

CK isoenzyme

76
Q

Catalyzed the interconversion of lactic and pyruvic acids
Widely distributed, highest activities in heart, hepatic, skeletal muscle and RBC

A

Lactate Dehydrogenase (LDH)

77
Q

Is a tetrameric molecule composed of 4 subunits/monomers of 2 possible forms

A

LDH

78
Q

lactate + NAD → ___

A

pyruvate + NADH + H

79
Q

Composed of 5 isoenzymes

A

LDH

80
Q

temp that decreases the activity of LD

A

low temp/freezer temp

81
Q

temp (+storage) that can maintain the activity of LD

A

If room temp for 2 days

82
Q

Assay of Enzyme Activity for LDH

A

Wacker method
Wroblewski La Due
a-hydroxybutyrate dehydrogenase (a-HBD)

83
Q

Reverse Reaction (Pyruvate → Lactate)
Decrease in absorbance is monitored at 340 nm
Three times faster but more susceptible to substrate exhaustion

A

Wroblewski La Due

84
Q

Optimal pH of Wroblewski La Due

A

7.1 to 7.4

85
Q

Forward reaction (Lactate → pyruvate)
Increase in absorbance is monitored at 340 nm
Commonly used method in LD

A

Wacker method

86
Q

Optimal pH of Wacker method

A

8.3 - 8.9

87
Q

Has greater affinity of H subunits

A

a-hydroxybutyrate dehydrogenase (a-HBD)

88
Q

Represent LDH-1

A

a-hydroxybutyrate dehydrogenase (a-HBD)

89
Q

a-ketobutyrate + NADH + H →

A

a-hydroxybutyrate

90
Q

After MI, LD begin to rise within ____, peak at ____ and remains elevated for ___

A

10-24 hrs; 48-72 hrs; 10 days

91
Q

Reference range of LD

A

100-225 U/L

92
Q

LDH is a __ containing two active sub-units

A

tetramer

93
Q

Order ng pinakamataas sa healthy serum

A

LD 2 > 1 > 3 > 4 > 5

94
Q

order of LD from most anodic (fastest) to least anodic (slowest)

A

LD 1 > LD 2 > LD 3 > LD 4 > LD 5

95
Q

🡹LDH 1 & 🡹CK-MB

A

AMI

96
Q

🡹LDH 1 and normal CK-MB

A

hemolytic anemia

97
Q

LDH 6 (Alcohol Dehydrogenase) present in px with:

A

Drug hepatotoxicity
Obstructive Jaundice
Artherosclerotic failure

98
Q

LDH-1 and LDH-2 tissue involved

A

Heart, RBC
1 - (MI, hemolytic anemia)
2 - (RI, megaloblastic anemia)

99
Q

LDH-3

A

Lung, Spleen, Pancreas (Pulmonary embolism)

100
Q

LDH-4

A

Liver (Hepatic injury)

101
Q

LDH-5

A

Skeletal Muscle (Skeletal muscle injury)

102
Q

Catalyze the hydrolysis of various phosphomonoesters at an alkaline pH
Liberate inorganic phosphate from an organic phosphate ester with production of alcohol

A

Alkaline phosphatase (ALP)

103
Q

Sources of ALP

A

Sources: Liver, Bone (Osteoblast), Placenta, Intestine, Renal tissues

104
Q

Requires Mg2+ activator
For evaluation of hepatobiliary and bone disorders

A

ALP

105
Q

Reference Range of ALP

A

30-90 U/L (adult)
70-220 u/L (0-3 months)
50-260 U/L (3-10 years)
60-295 U/L (10-puberty)

106
Q

Assay for enzyme activity
in ALP

A

Bowers and McComb

107
Q

Based on molar absorptivity of P-Nitrophenol at a pH of 10.2
Absorbance is measured at 405 nm (visible light region)

A

Bowers and McComb

108
Q

p-nitrophenyl-phosphate (colorless) → ___

A

p-nitrophenol + phosphate ion (yellow)

109
Q

methods with β-glycero-phosphate as substrate

A

Bodansky
Shinowara
Jones
Reinhart

110
Q

methods with P-nitrophenyl phosphate as substrate

A

Bessy, Lowry & Brock
Bowers & McComb

111
Q

method in which phenyl phosphate as substrate

A

King and Armstrong

112
Q

methods where
Inorganic PO4 + Glycerol as end product

A

Bodansky
Shinowara
Jones
Reinhart

113
Q

P-nitrophenol (yellow)
as end product

A

Bessy, Lowry & Brock
Bowers & McComb

114
Q

end product of King and Armstrong

A

Phenol

115
Q

ALP Isoenzymes:

A

Electrophoresis

116
Q

Electrophoresis - Arranged by most anodal (fastest)

A
  1. Liver ALP - fastest
  2. Bone ALP
  3. Placental ALP
  4. Intestinal ALP
117
Q

Heat labile fraction
🡹 in bone disease, healing of bone fractures, and physiologic bone growth

A

Bone ALP

118
Q

Fastest Isoenzyme and 🡹 in liver disease
Two fractions: Major liver & fast liver (a1) band

A

Liver ALP

119
Q

Most heat stable fraction and 🡹 in pregnancy
Can withstand heating at 65degC for 30 mins

A

Placental ALP

120
Q

Slowest moving fraction, in blood groups B or O
🡹 in fatty meal consumption and GIT disorders

A

Intestinal ALP

121
Q

Chemical inhibition in ALP:
Phenylalanine

A

Placental, Intestinal (Putang Ina)

122
Q

Chemical inhibition in ALP:
Levamisole

A

Bone, Liver (Blood Lust ♥)

123
Q

Chemical inhibition in ALP:
.03 moral urea

A

Bone (only one to be inhibited)

124
Q

ALP isoenzyme differentiation by Heat stability

A

Placental ALP (most stable)
Intestinal ALP
Liver ALP
Bone ALP (least stable)

125
Q

Total ALP elevations by liver or bone ALP is differentiated by heating of serum at ___

A

56degC for 10 mins

126
Q

ALP residual activity is ⬇ decrease to >20%

A

Liver ALP

127
Q

ALP residual activity is ⬇ decrease to <20%

A

Bone ALP

128
Q

Carcino Placental ALP

A

Regan ALP:
Nagao ALP

129
Q

Carcino Placental ALP Inhibitors:

A

phenylalanine, L-leucine

130
Q

Most heat stable ALP
Lung, Breast, and Gynecological cancers, bone ALP co-migrator,

A

Regan ALP

131
Q

Adenocarcinoma of the pancreas and bile duct, pleural cancer

A

Nagao ALP

132
Q

INHIBITED BY:
Phenylalanine
L-leucine

A

Nagao

133
Q

INHIBITED BY:
Phenylalanine

A

Regan

134
Q

Catalyze the hydrolysis of various phosphomonoesters at an acid pH
Liberate inorganic phosphate from an organic phosphate ester with production of alcohol

A

Acid phosphatase (ACP)

135
Q

Acid phosphatase is present in the ff tissue source:

A

Prostate
Red blood cells
Platelets
Bone

136
Q

For evaluation of metastatic carcinoma of prostate
Forensic investigation of rape

A

ACP

137
Q

inhibits specific prostatic ACP

A

L-tartrate ions

138
Q

Reference Range: Prostatic ACP:

A

0-3.5 ng/ml

139
Q

Quantitative end point substrate

A

Thymolphthalein monophosphate

140
Q

Continuous monitoring substrate

A

α-napthyl phosphate

141
Q

Gutman and Gutman substrate and end product

A

Phenyl PO4;
Inorganic phosphate

142
Q

Shinowara substrate and end product

A

PNPP;
P-Nitrophenol

143
Q

Babson, Read, and Phillips substrate and end product

A

Alpha naphtyl PO4;
Alpha naphthol

144
Q

Roy and Hillman substrate and end product

A

Thymolphthalein MonoPO4
Free thymolphthalein

145
Q

where pancreatic enzymes r produced

A

acinar cells of the pancreas

146
Q

An example of HYDROLASE
Promotes breakdown of starch and glycogen via alpha, 1-6 branching linkages

A

Amylase (AMS)

147
Q

Major tissue source of AMS

A

Pancreas
Salivary gland

148
Q

Minor tissue source of AMS

A

Adipose tissues
Fallopian tube
Small intestine
Skeletal muscle

149
Q

Increased in acute pancreatitis, renal failure, and parotitis
Is the smallest enzyme
The first enzyme to increase in acute pancreatitis

A

AMS

150
Q

Amylase increases after ____, the peak is after ___. The level persists for .

A

2-12 hours; 24 hours; 3-5 days

151
Q

Salivary amylase - __

A

ptyalin (fast moving)

152
Q

Pancreatic amylase -__

A

amylopsin (slow moving)

153
Q

The activity of amylase is inversely proportional with the absorbance
Measures the disappearance of starch substrate
Starch-Iodine complex (dark-blue) 🡺 Decrease in color intensity (decreased absorbance)

A

Amyloclastic

154
Q

Measures the appearance of the product
Starch 🡺 reducing sugars
Directly proportional of amylase activity with the absorbance

A

Saccharogenic

155
Q

Measures the increasing color from production of product-chromogenic dye fragment
Insoluble starch-dye 🡺 double starch-dye fragments
Amylase activity is directly proportional to the starch-dye fragment formation

A

Chromogenic

156
Q

Coupling of several enzyme systems to monitor amylase activity
The end product is the 5,6-phosphogluconolactone + 5 NADH (🡹 absorbance)

A

Continuous monitoring

157
Q

maltopentose → ___

A

maltrotriose + maltose

158
Q

Not excreted and is reabsorb in the plasma
Presence of macroamylase in the plasma
Amylase with antibodies

A

Macroamylasemia

159
Q

Hydrolyzes the ester linkages of fats to produce alcohols and fatty acids
Hydrolysis of dietary triglycerides in the intestine to 2-monoglyceride and fatty acids

A

Lipase (LPS)

160
Q

Specific for pancreatitis
But in time of elevation, amylase is faster than ___

A

LPS

161
Q

2-monoglyceride + 2 fatty acids → ___

A

triacylglycerol + 2H2O

162
Q

Larger molecule and remains longer in circulation (7 days)

A

LPS

163
Q

Assay for enzyme activity LPS
Estimation of liberated fatty acids
Measurement of the amount of light blocked by the suspension or particles in soluble agents in the sample.

A

Turbidimetric methods

164
Q

method where phenolphthalein as indicator for LPS

A

Cherry Crandall

165
Q

Tietz indicator

A

Thymolphthalein + Veronal

166
Q

end color of Cherry Crandall

A

Pink

167
Q

end color of Tietz

A

Blue

168
Q

Cherry Crandall & Tietz’s substrate

A

50% olive oil (triolein)

169
Q

titrating agent for Cherry and Tietz

A

0.4N NaOH

170
Q

end point of Cherry and Tietz

A

Fatty acid (Oleic acid)

171
Q

A phosphoric monoester hydrolase
Marker for hepatobiliary disease and lesions of liver
Reference value: 0-1.6 units

A

5’ Nucleotidase (5’N)

172
Q

Used as a marker for insecticides/pesticides poisoning
Index of parenchymal function

A

Cholinesterase / Pseudocholinesterase

173
Q

Used to monitor the effect of muscle relaxants (succinylcholine) after surgery
Reference value: 0.5 - 1.3 Units (plasma)

A

Cholinesterase / Pseudocholinesterase

174
Q

Used as a possible indicator of neuronal dysfunction (ptx w/ alzheimer’s disease)
Conversion of Angiotensin 1 to 2 happens in the lungs

A

Angiotensin-Converting enzyme (ACE)

175
Q

A.K.A. Peptidyl Dipeptidase A or Kininase II
Increased in: Sarcoidosis, Acute and Chronic Bronchitis, and Leprosy

A

Angiotensin-Converting enzyme (ACE)

176
Q

main source of ACE

A

Main source: Macrophage and Epithelioid cells

177
Q

Promotes the vasoconstriction of the renal arterioles to promote increase BP
Stimulates the release of aldosterone

A

Angiotensin II

178
Q

Copper-carrying protein which acts as a na enzyme
A marker for wilson’s disease (hepatolenticular disease)

A

Ceruloplasmin

179
Q

For hepatobiliary diseases
Reference values: 8-20 mU/ml

A

Ornithine carbamoylTransferase (OCT)

180
Q

maintains the NADPH in the reduced form in erythrocytes
a newborn screening marker

A

Glucose-6-phosphate dehydrogenase (G-6PD)

181
Q

Maintains the NADPH in the reduced form in the erythrocytes
A newborn screening marker

A

Glucose-6-phosphate dehydrogenase (G-6PD)

182
Q

Deficiency can lead to drug-induced
Specimen: red cell hemolysate, serum
Reference value : 10-15 U/g Hgb or 1200-2000 mU/mL packed RBC

A

Glucose-6-phosphate dehydrogenase (G-6PD)

183
Q

Glucose-6-phosphate dehydrogenase (G-6PD) is found in the

A

adrenal cortex, spleen, rbc, and lymph nodes

184
Q

Increased levels of G6PD can be seen in conditions like:

A

AMI, megaloblastic anemia

185
Q

inhibits red cell ACP

A

Formaldehyde & Cupric ions

CC MTAP2 (1 decks)

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